Lengthening the Guanidine-Aryl Linker of Phenylpyrimidinylguanidines Increases Their Potency as Inhibitors of FOXO3-Induced Gene Transcription.


Journal

ACS omega
ISSN: 2470-1343
Titre abrégé: ACS Omega
Pays: United States
ID NLM: 101691658

Informations de publication

Date de publication:
27 Sep 2022
Historique:
received: 21 07 2022
accepted: 07 09 2022
entrez: 3 10 2022
pubmed: 4 10 2022
medline: 4 10 2022
Statut: epublish

Résumé

Increased FOXO3 nuclear localization is involved in neuroblastoma chemoresistance and tumor angiogenesis. Accordingly, FOXO3 inhibition is a promising strategy for boosting antitumor immune responses and suppressing FOXO3-mediated therapy resistance in cancer cells. However, no FOXO3 inhibitors are currently available for clinical use. Nevertheless, we have recently identified (4-propoxy)phenylpyrimidinylguanidine as a FOXO3 inhibitor in cancer cells in the low micromolar range. Here, we report the synthesis and structure-activity relationship study of a small library of its derivatives, some of which inhibit FOXO3-induced gene transcription in cancer cells in a submicromolar range and are thus 1 order of magnitude more potent than their parent compound. By NMR and molecular docking, we showed that these compounds differ in their interactions with the DNA-binding domain of FOXO3. These results may provide a foundation for further optimizing (4-propoxy)phenylpyrimidinylguanidine and developing therapeutics for inhibiting the activity of forkhead box (FOX) transcription factors and their interactions with other binding partners.

Identifiants

pubmed: 36188303
doi: 10.1021/acsomega.2c04613
pmc: PMC9521028
doi:

Types de publication

Journal Article

Langues

eng

Pagination

34632-34646

Informations de copyright

© 2022 The Authors. Published by American Chemical Society.

Déclaration de conflit d'intérêts

The authors declare no competing financial interest.

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Auteurs

Klara Kohoutova (K)

Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Albertov 6, Prague 12843, Czech Republic.
Institute of Physiology of the Czech Academy of Sciences, Laboratory of Structural Biology of Signaling Proteins, Division BIOCEV, Prumyslova 595, Vestec 25250, Czech Republic.

Vojtěch Dočekal (V)

Department of Organic Chemistry, Faculty of Science, Charles University, Albertov 6, Prague 12843, Czech Republic.

Michael J Ausserlechner (MJ)

Department of Pediatrics I, Medical University Innsbruck, Innrain 66, Innsbruck 6020, Austria.

Nora Kaiser (N)

Department of Pediatrics I, Medical University Innsbruck, Innrain 66, Innsbruck 6020, Austria.

Andrej Tekel (A)

Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Albertov 6, Prague 12843, Czech Republic.

Raju Mandal (R)

Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Albertov 6, Prague 12843, Czech Republic.

Matej Horvath (M)

Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Albertov 6, Prague 12843, Czech Republic.

Veronika Obsilova (V)

Institute of Physiology of the Czech Academy of Sciences, Laboratory of Structural Biology of Signaling Proteins, Division BIOCEV, Prumyslova 595, Vestec 25250, Czech Republic.

Jan Vesely (J)

Department of Organic Chemistry, Faculty of Science, Charles University, Albertov 6, Prague 12843, Czech Republic.

Judith Hagenbuchner (J)

Department of Pediatrics II, Medical University Innsbruck, Innrain 66, Innsbruck 6020, Austria.

Tomas Obsil (T)

Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Albertov 6, Prague 12843, Czech Republic.
Institute of Physiology of the Czech Academy of Sciences, Laboratory of Structural Biology of Signaling Proteins, Division BIOCEV, Prumyslova 595, Vestec 25250, Czech Republic.

Classifications MeSH